Essentially all known human cancers have been characterized by aberrant glycosylation occurring in lipids (glycosphingolipids) or in proteins (glycoproteins) expressed at the cell surface membrane (Hakomori, S. (1985) Cancer Res. 45, 2405-2414). Aberrant glycosylation in human cancer has been indicated by the presence of a large quantity of novel fucosylated glycolipids detected by chemical analysis (Hakomori, S. and Andrews, H. (1970) Biochim. Biophys. Acta 202, 225-228; Yang, H.-J., and Hakomori, S. (1971) J. Biol. chem. 246, 1192-1200; Hakomori, S. et al. (1984) J. Biol. Chem. 259, 4672-4680; Nudelman, E. et al. (1986) J. Biol. Chem. 261, 11247-11253), and by the fact that many monoclonal antibodies selected by preferential or specific reactivity with human cancer have been characterized as being directed to glycophingolipids or glycoproteins (Nudelman, E., et al., (1986) J. Biol. Chem. 261, 11247-11253; Magnani, J. L. et al. (1982) J. Biol. Chem. 257, 14365-14369; Fukushi, Y., et al. (1984) J. Biol. Chem. 259, 4681-4685 and Fukushi, Y. et al. (1984) J. Biol. Chem. 259, 10511-10517; see Hakomori, S. (1985) Cancer Res. 45, 2405-2414 and Hakomori, S. (1984) Ann. Rev. Immunol. 2, 103-126 for a review). The characteristic change occurring in the most common human cancers (i.e. gastrointestinal, breast and lung cancers) is the accumulation of large quantities of fucosylated type 1 and 2 chains (Le.sup.a, Le.sup.x, di- or trimeric Le.sup.x, Le.sup.b, Le.sup.y) or their sialylated derivatives (sialyl Le.sup.x, sialyl di- or trimeric Le.sup.x, sialyl Le.sup.a) defined by various monoclonal antibodies (Yang. H.-J. and Hakomori, S. (1971) J. Biol. Chem. 246, 1192-1200; Hakomori, S. et al. (1986) J. Biol. Chem. 259, 4672-4680; Nudelman, E. et al., (1986) J. Biol. Chem. 261, 11247-11253; Magnani, J. L. et al. (1982) J. Biol. Chem. 257, 14365-14369g; Fukushi, Y. et al. (1984) J. Biol. Chem. 259, 4681-4685; Fukushi, Y. et al. (1984) J. Biol. Chem. 259, 10511-10517; see Hakomori, S. (1984) Ann. Rev. Immunol. 2, 103-126 for a review).
Because such fucosylated molecules could be useful for preparing antibodies directed to human cancer associated antigens and even as a vaccine for immunization against some cancers, isolation and characterization of such fucosylated structures and their antigenic determinants is an important aspect of cancer research.